Online citations, reference lists, and bibliographies.
← Back to Search

Dystrophin, Vinculin, And Aciculin In Skeletal Muscle Subject To Chronic Use And Disuse.

M. Rezvani, O. Ornatsky, Michael K. Connor, H. A. Eisenberg, D. Hood
Published 1996 · Medicine

Cite This
Download PDF
Analyze on Scholarcy
Share
Dystrophin is a subsarcolemmal protein that interacts with cytoskeletal actin and a glycoprotein complex in the plasma membrane. One potential function of dystrophin is its ability to stabilize the sarcolemmal membrane during muscle contraction. We hypothesized 1) that chronic muscle use and disuse would alter the expression of dystrophin as a compensatory mechanism designed to prevent muscle damage, and 2) that other subsarcolemmal cytoskeletal proteins (vinculin, M-vinculin, aciculin 60/63 kDa) that colocalize with dystrophin in muscle adherens junctions would be changed in parallel. Chronic muscle use induced by voluntary running or 10-Hz chronic stimulation did not alter dystrophin levels in rat muscle. In contrast, muscle disuse induced by 6 d of microgravity, or 7 and 21 d of denervation, increased dystrophin levels by 1.8-, 1.9- and 3.2-fold, respectively. Thus, this increase in dystrophin levels appears to be dependent on the duration of muscle disuse, independent of the presence of the nerve. Denervation also induced 3.3-fold increases in vinculin and aciculin 60 kDa, in parallel with dystrophin. However, in contrast to its effects on dystrophin, chronic stimulation increased the levels of vinculin and aciculin 60 kDa by 3.4- and 6.4-fold, respectively. Thus, both the removal and the augmentation of muscle activity resulted in increases of these two cytoskeletal proteins. The data indicate that the concentrations of these proteins are independently regulated. They further indicate that chronic muscle use is not a stimulus for the induction of dystrophin levels, suggesting that normal levels are sufficient for the protective effect on the sarcolemma that dystrophin may confer. The results reveal an interesting area of muscle plasticity, and the adaptation observed may have profound implications for the structure and function of skeletal muscle responding to changes in contractile activity.
This paper references
10.1152/JAPPL.1993.74.2.942
Portable electrical stimulator for use in small animals.
M. Takahashi (1993)
10.1111/J.1432-1033.1991.TB16428.X
Analysis of excitation-contraction-coupling components in chronically stimulated canine skeletal muscle.
K. Ohlendieck (1991)
10.1002/MUS.880170103
Dystrophin–glycoprotein complex: Its role in the molecular pathogenesis of muscular dystrophies
K. Matsumura (1994)
10.1002/j.1460-2075.1988.tb03076.x
Porcine vinculin and metavinculin differ by a 68‐residue insert located close to the carboxy‐terminal part of the molecule.
M. Gimona (1988)
10.1016/0014-5793(92)80615-N
Quantitative analysis of dystrophin in fast‐ and slow‐twitch mammalian skeletal muscle
M. A. Ho-Kim (1992)
10.1016/0014-5793(86)80027-8
Meta‐vinculin distribution in adult human tissues and cultured cells
M. Glukhova (1986)
10.1152/JAPPL.1994.76.2.859
Blood flow, mitochondria, and performance in skeletal muscle after denervation and reinnervation.
H. A. Eisenberg (1994)
10.1007/BFB0036123
Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation.
D. Pette (1992)
A novel phosphoglucomutase-related protein is concentrated in adherens junctions of muscle and nonmuscle cells.
A. Belkin (1994)
10.1042/CS0840145
Progressive deterioration of muscles in mdx mice induced by overload.
J. Dick (1993)
10.1152/JAPPL.1987.63.6.2549
Induction of voluntary prolonged running by rats.
J. C. Russell (1987)
10.1152/JAPPL.1990.68.4.1481
Biochemical transformation of canine skeletal muscle for use in cardiac-assist devices.
C. D. Ianuzzo (1990)
10.1111/J.1432-1033.1989.TB14551.X
Chronic stimulation of rat skeletal muscle induces coordinate increases in mitochondrial and nuclear mRNAs of cytochrome-c-oxidase subunits.
D. Hood (1989)
Protein measurement with the Folin phenol reagent.
O. H. Lowry (1951)
10.1007/3540528806_3
Cellular and molecular diversities of mammalian skeletal muscle fibers.
D. Pette (1990)
10.1139/H94-002
Mitochondrial biogenesis in striated muscle.
D. Hood (1994)
10.1126/SCIENCE.1439807
Cytoskeleton--plasma membrane interactions.
E. Luna (1992)
10.1007/BF01738325
What does dystrophin do in normal muscle?
J. Lansman (2005)
Expression and localization of the phosphoglucomutase-related cytoskeletal protein, aciculin, in skeletal muscle.
A. Belkin (1994)
10.1083/JCB.115.2.411
The subcellular distribution of dystrophin in mouse skeletal, cardiac, and smooth muscle
T. Byers (1991)
10.1083/JCB.117.5.997
Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle
G. Porter (1992)
Coordinate changes in fast thin filament and Z-line protein expression in the early response to chronic stimulation.
F. Schachat (1988)
10.1152/JAPPL.1993.74.2.934
Chronic stimulation-induced changes in mitochondria and performance in rat skeletal muscle.
M. Takahashi (1993)
10.1042/BJ2690503
Co-ordinate expression of cytochrome c oxidase subunit III and VIc mRNAs in rat tissues.
D. Hood (1990)
10.1016/0003-2697(87)90406-4
A two-step procedure for efficient electrotransfer of both high-molecular-weight (>400,000) and low-molecular-weight (<20,000) proteins☆
T. Otter (1987)
10.1083/JCB.122.4.809
A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
J. Ervasti (1993)
10.1002/CM.970200102
The cytoplasmic domain of adherens-type junctions.
B. Geiger (1991)



This paper is referenced by
10.1016/S1569-2574(08)60006-4
Is skeletal muscle ready for long-term spaceflight and return to gravity?
D. Riley (1999)
10.1016/S0928-4680(98)80770-0
The disruption of myofibre structures in skeletal muscle after forced lengthening contractions
J. Komulainen (1998)
10.1101/2020.06.30.179465
Recurrent training rejuvenates and enhances transcriptome and methylome responses in young and older human muscle
S. Blocquiaux (2020)
10.1023/B:JURE.0000035893.59267.47
Function Induced Modifications of Gene Expression: an Alternative Approach to Gene Therapy of Duchenne Muscular Dystrophy
G. Vrbóva (2004)
10.1152/ajpcell.00181.2010
Effect of denervation-induced muscle disuse on mitochondrial protein import.
Kaustabh Singh (2011)
10.1152/AJPCELL.00529.2001
Dystrophin-glycoprotein complex and Ras and Rho GTPase signaling are altered in muscle atrophy.
P. Chockalingam (2002)
10.2486/INDHEALTH.42.401
Effects of static load on the weight and protein content in the leg muscles of the mouse: a simulation of prolonged standing in the workplace.
S. Ueno (2004)
10.1002/(SICI)1097-4598(200004)23:4<590::AID-MUS19>3.0.CO;2-Z
Membrane skeleton of innervated and denervated fast‐ and slow‐twitch muscle
M. W. Williams (2000)
10.1152/AJPREGU.2001.280.2.R323
Cytoskeletal protein contents before and after hindlimb suspension in a fast and slow rat skeletal muscle.
A. Chopard (2001)
mitochondrial protein import Effect of denervation-induced muscle disuse on
Kaustabh Singh (2011)
10.1152/AJPCELL.1997.273.1.C297
Early functional and biochemical adaptations to low-frequency stimulation of rabbit fast-twitch muscle.
A. Hicks (1997)
10.1242/jcs.152157
Aciculin interacts with filamin C and Xin and is essential for myofibril assembly, remodeling and maintenance
Sibylle Molt (2014)
10.1159/000091270
Distribution of Costameric Proteins in the Diaphragm of Patients with Chronic Obstructive Pulmonary Disease
J. Wijnhoven (2006)
10.1016/S0165-0173(99)00090-9
Brain dystrophin, neurogenetics and mental retardation
M. Mehler (2000)
10.1016/S0006-291X(02)02898-X
Increased expression of the nicotinic acetylcholine receptor in stimulated muscle.
Clare O’Reilly (2003)
10.1007/s10974-007-9102-0
Repeated bout effect on the cytoskeletal proteins titin, desmin, and dystrophin in rat skeletal muscle
T. Lehti (2007)
10.1007/s00424-002-0872-3
Vinculin and meta-vinculin in fast and slow rat skeletal muscle before and after hindlimb suspension
A. Chopard (2002)
10.1007/s004240050696
The disruption of myofibre structures in rat skeletal muscle after forced lengthening contractions
J. Komulainen (1998)
Semantic Scholar Logo Some data provided by SemanticScholar